The effect of high pressure on thermolysin
作者： Shigeru Kunugi , Moto Kitayaki , Yuuichi Yanagi , Naoki Tanaka , Reinhard Lange
DOI: 10.1111/J.1432-1033.1997.T01-1-00567.X
关键词:
摘要: The effects of high pressure on thermolysin activity and spectroscopic properties were studied. Thermolysin showed distinct pressure-induced activation with a maximum observed at 200-250 MPa for dipeptide amide substrate 100-120 heptapeptide substrate. By examining the dependence hydrolytic rate former using stopped-flow apparatus as mixing device under elevated pressures, volume reaction was -71 ml mol(-1) 25 degrees C. Delta V++ accompanied by negative expansibility value -95 obtained 45 A prolonged incubation pressure, however, caused time-dependent deactivation. These changes due to monitored several methods. fourth-derivative absorbance spectrum an irreversible change, mostly in tyrosine tryptophan regions, higher than 300 MPa. Intrinsic fluorescence circular dichroism measurements solution also detected changes. All these indicated that change occurred pressures are explained simple two-state transition model large, reaction.
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